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ZNFX1_CAEEL
ID   ZNFX1_CAEEL             Reviewed;        2443 AA.
AC   E9P860; Q23388;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=NFX1-type zinc finger-containing protein 1 homolog {ECO:0000312|WormBase:ZK1067.2b};
DE            EC=3.6.4.13 {ECO:0000305|PubMed:29775580};
GN   Name=znfx-1 {ECO:0000303|PubMed:29775580, ECO:0000312|WormBase:ZK1067.2b};
GN   ORFNames=ZK1067.2 {ECO:0000312|WormBase:ZK1067.2b};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH EGO-1; CSR-1; WAGO-1 AND
RP   PRG-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-1067; LEU-1530 AND TYR-1562.
RX   PubMed=29775580; DOI=10.1016/j.molcel.2018.04.009;
RA   Ishidate T., Ozturk A.R., Durning D.J., Sharma R., Shen E.Z., Chen H.,
RA   Seth M., Shirayama M., Mello C.C.;
RT   "ZNFX-1 Functions within Perinuclear Nuage to Balance Epigenetic Signals.";
RL   Mol. Cell 70:639-649(2018).
RN   [3] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH WAGO-4, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ARG-271; LEU-290;
RP   407-ARG--LEU-2443; ALA-1047; LYS-1067; HIS-1504; LEU-1530 AND TYR-1562.
RX   PubMed=29769721; DOI=10.1038/s41586-018-0132-0;
RA   Wan G., Fields B.D., Spracklin G., Shukla A., Phillips C.M., Kennedy S.;
RT   "Spatiotemporal regulation of liquid-like condensates in epigenetic
RT   inheritance.";
RL   Nature 557:679-683(2018).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=32843637; DOI=10.1038/s41467-020-18089-1;
RA   Suen K.M., Braukmann F., Butler R., Bensaddek D., Akay A., Lin C.C.,
RA   Milonaityte D., Doshi N., Sapetschnig A., Lamond A., Ladbury J.E.,
RA   Miska E.A.;
RT   "DEPS-1 is required for piRNA-dependent silencing and PIWI condensate
RT   organisation in Caenorhabditis elegans.";
RL   Nat. Commun. 11:4242-4242(2020).
CC   -!- FUNCTION: Epigenetic inheritance factor which, in association with the
CC       Argonaute protein wago-4, mediates small RNA-directed transgenerational
CC       epigenetic inheritance and thus balances the transgenerational
CC       inheritance of epigenetic information (PubMed:29775580,
CC       PubMed:29769721). Specifically, maintains a balanced production of
CC       small RNAs by preventing the spread of epigenetic signals towards the
CC       5'-end of target mRNAs (PubMed:29775580). Plays a role in small RNA-
CC       induced gene silencing in the germline (PubMed:29775580).
CC       {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000305|PubMed:29775580};
CC   -!- SUBUNIT: Interacts with ego-1, csr-1, wago-1 and prg-1
CC       (PubMed:29775580). Interacts with wago-4; the interaction promotes the
CC       transmission of epigenetic information across generations
CC       (PubMed:29769721). {ECO:0000269|PubMed:29769721,
CC       ECO:0000269|PubMed:29775580}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580}. Cytoplasm
CC       {ECO:0000269|PubMed:29775580}. Cytoplasmic granule
CC       {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580,
CC       ECO:0000269|PubMed:32843637}. Note=Co-localizes with wago-4 in P-
CC       granules in germline blastomeres until the 100-cell stage
CC       (PubMed:29769721). During oocyte maturation, co-localizes with wago-4
CC       in liquid-like condensates in the cytoplasm called Z granules
CC       (PubMed:29769721). Localizes to perinuclear and cytoplasmic P-granules
CC       in germline blastomeres and germ cells (PubMed:29775580,
CC       PubMed:29769721). In the adult germline, co-localizes with deps-1 in P-
CC       granules (PubMed:32843637). {ECO:0000269|PubMed:29769721,
CC       ECO:0000269|PubMed:29775580, ECO:0000269|PubMed:32843637}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=b {ECO:0000312|WormBase:ZK1067.2b};
CC         IsoId=E9P860-1; Sequence=Displayed;
CC       Name=a {ECO:0000312|WormBase:ZK1067.2a};
CC         IsoId=E9P860-2; Sequence=VSP_060387;
CC   -!- TISSUE SPECIFICITY: Expressed in germs cells (PubMed:29775580,
CC       PubMed:29769721). Not expressed in somatic tissues (PubMed:29769721).
CC       {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in germ cells at all stages of
CC       development. {ECO:0000269|PubMed:29769721,
CC       ECO:0000269|PubMed:29775580}.
CC   -!- DISRUPTION PHENOTYPE: Defective RNA-induced gene silencing.
CC       {ECO:0000269|PubMed:29775580}.
CC   -!- SIMILARITY: Belongs to the ZNFX1 family. {ECO:0000305}.
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DR   EMBL; BX284602; CAA93884.2; -; Genomic_DNA.
DR   EMBL; BX284602; CBZ01828.1; -; Genomic_DNA.
DR   RefSeq; NP_001254204.1; NM_001267275.1.
DR   RefSeq; NP_001254205.1; NM_001267276.1.
DR   AlphaFoldDB; E9P860; -.
DR   SMR; E9P860; -.
DR   STRING; 6239.ZK1067.2b; -.
DR   EPD; E9P860; -.
DR   PaxDb; E9P860; -.
DR   PeptideAtlas; E9P860; -.
DR   EnsemblMetazoa; ZK1067.2a.1; ZK1067.2a.1; WBGene00014208. [E9P860-2]
DR   EnsemblMetazoa; ZK1067.2a.2; ZK1067.2a.2; WBGene00014208. [E9P860-2]
DR   EnsemblMetazoa; ZK1067.2b.1; ZK1067.2b.1; WBGene00014208. [E9P860-1]
DR   UCSC; ZK1067.2; c. elegans.
DR   WormBase; ZK1067.2a; CE43256; WBGene00014208; znfx-1. [E9P860-2]
DR   WormBase; ZK1067.2b; CE45745; WBGene00014208; znfx-1. [E9P860-1]
DR   eggNOG; KOG1807; Eukaryota.
DR   GeneTree; ENSGT00940000160694; -.
DR   HOGENOM; CLU_233183_0_0_1; -.
DR   InParanoid; E9P860; -.
DR   OMA; CHPNVEY; -.
DR   OrthoDB; 271662at2759; -.
DR   PhylomeDB; E9P860; -.
DR   PRO; PR:E9P860; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00014208; Expressed in adult organism and 3 other tissues.
DR   GO; GO:0031380; C:nuclear RNA-directed RNA polymerase complex; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0031048; P:heterochromatin assembly by small RNA; IBA:GO_Central.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; -; 3.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000967; Znf_NFX1.
DR   PANTHER; PTHR10887; PTHR10887; 2.
DR   Pfam; PF13086; AAA_11; 2.
DR   Pfam; PF13087; AAA_12; 1.
DR   SMART; SM00438; ZnF_NFX; 4.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Helicase; Hydrolase;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Repeat; RNA-binding;
KW   RNA-mediated gene silencing; Zinc; Zinc-finger.
FT   CHAIN           1..2443
FT                   /note="NFX1-type zinc finger-containing protein 1 homolog"
FT                   /id="PRO_0000448351"
FT   DOMAIN          1040..1545
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   ZN_FING         1769..1791
FT                   /note="NF-X1-type 1"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         1853..1873
FT                   /note="NF-X1-type 2"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         1912..1930
FT                   /note="NF-X1-type 3"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         2027..2044
FT                   /note="NF-X1-type 4"
FT                   /evidence="ECO:0000255"
FT   REGION          212..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..292
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1061..1068
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   VAR_SEQ         1..231
FT                   /note="Missing (in isoform a)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060387"
FT   MUTAGEN         271
FT                   /note="R->C: In gg483; disrupted inheritance of RNA-induced
FT                   gene silencing."
FT                   /evidence="ECO:0000269|PubMed:29769721"
FT   MUTAGEN         290
FT                   /note="L->F: In gg502; disrupted inheritance of RNA-induced
FT                   gene silencing."
FT                   /evidence="ECO:0000269|PubMed:29769721"
FT   MUTAGEN         407..2443
FT                   /note="Missing: In gk458570; disrupted inheritance of RNA-
FT                   induced gene silencing."
FT                   /evidence="ECO:0000269|PubMed:29769721"
FT   MUTAGEN         1047
FT                   /note="A->T: In gg511; disrupted inheritance of RNA-induced
FT                   gene silencing."
FT                   /evidence="ECO:0000269|PubMed:29769721"
FT   MUTAGEN         1067
FT                   /note="K->A: In ne4382; defective RNA-induced gene
FT                   silencing."
FT                   /evidence="ECO:0000269|PubMed:29775580"
FT   MUTAGEN         1504
FT                   /note="H->Y: In gg509; disrupted inheritance of RNA-induced
FT                   gene silencing."
FT                   /evidence="ECO:0000269|PubMed:29769721"
FT   MUTAGEN         1530
FT                   /note="L->F: In ne4338 and ne4449; viable and fertile.
FT                   Defective RNA-induced gene silencing."
FT                   /evidence="ECO:0000269|PubMed:29775580"
FT   MUTAGEN         1562
FT                   /note="Y->C: In ne4415 and ne4450; viable and fertile.
FT                   Defective RNA-induced gene silencing at 24 degrees
FT                   Celsius."
FT                   /evidence="ECO:0000269|PubMed:29775580"
SQ   SEQUENCE   2443 AA;  280315 MW;  D7F25167F9E5F413 CRC64;
     MSRDKPPQRE VGGRRLPYEM GSLKFDEDPF RGQRRRPWMC FRIGYPTSEF SSEHFMKFVK
     RCHTSMIEVG ILLDDEREFL QYQEVREDYL LLKKLIEEGL QKCETIYEKG PLSTPVVFFI
     LDQCDEDEVQ NMLDMFRESC YIFHMKRNEI LNWINEMEYE ELESDCSKFA QFIKGVENLT
     ESIAMPMEVE TEEFIFGKSS IVSTEDFVED APHKQIAQDQ RETRPIRQPY SMVRNLAPPG
     LPPPGISISN SSPPGLSSVS PIPRADTRES RYSTPQPPGL SIPAPPGISL PTPPGISLQN
     HQNDQFEQAH STISRMSENS SSSRRRFRDE EVQEEEGDHI LSSEDVHAAR NVCETKILVR
     GVPQKNDSEL SKLINGSKLY VRFERPFVKL AHNLELLYVV NYAISSRKSI VRDHSKAIIR
     GLFEKDFLLK LKSKFLESSF DNDTWTPEGT ELLFEIFHLF FTTARYKGGF MLTLPRFAPS
     WHDFSMAFDI ADMDGLEEAG VGDDELRNLR RLIGYIETWI KRAERERNPS PLALRSYSVY
     EKAGSSDSGR QVLSESRGAG SSNVYGHDEV DFVDHRRRDE FGHRDNYRTE NRRHKSPDNF
     GEVHRRLDEQ QQQRHEDESS RYRDDSRQSR RADDRRDQYQ YNESTSMENH LGFHNGGGTV
     SEHSRDDKFV SPQNCEEKRK YCEEDTDAKP QQPYRFEEIK FEPIWVKCEK SEPPEDFKTL
     PSVPVLSEYV NPVEPYLRRI QDDGKYKSVH HYLDVQFRLL KEDLVSPLRD GIDLYKKNGT
     CKGRRIEGAP CSDISIFNVE KVDGKQVTER DGYEMRIIWP AQYDILKLLD NDREMKELGL
     VMLSCDRFKE DFHLGHIQSS YLMRNGSLHF AVHEETSPFK PNTTYQMAQG TSYLPCYKHV
     LENLKRISSF KPLPFERYLV HGSKIIFRPN FQQAEKSEYQ ISEEKKLMKT YNELRSLAAC
     ARYTKGKPIP RGVDDDDEDY EFSKSRELSK EDIDLEYRQL QEPIFRPLVG VDIKDSNLIQ
     INKKWYNVSR LLDEFHPDYM DESQRLAFCN TFKYELSLIQ GPPGTGKTHI GVQIVKTILQ
     NRSYWKITEP ILVVCFTNSG LDNLLERIYQ MIENDEELSK DNGRPKIIRF GSKCDSNYLK
     RQNVMRQDVY EQYKSKVSDG AQKKMSKAGA ARRHKADNLA ISSYTLFCSR NKLLSYEMLS
     RVMDPNHQME IQQFTYDHVD TKGIPLSPDE AIGCWLLERD FGKATKSQTK KAKKPKFQGA
     QLDSEDENKD YFTVEDSDDE EDELDDEKLL DKLFEKMNLE CSGADILSAV HASHADEYYT
     KGPWEIVQDK RPSVVVLMEK KTKPCNAKFT VDEQINNLVS EIKDMILSSQ PVPKKDLNDI
     KYIFSLARLK RWSLYITWCD ALRSIVTENL PRQIREYREA CENFKNAQNR VDAEIMRMTM
     IIGATTTGCS RLRPTLEKVG PRILIVEEAA EVLEAHIISA MISTVEHVVM IGDHKQLRPN
     PAVHELGVAY GLRISMFERL VERGLPFSQL RQQHRMNLTI SDKIVKLSFY DNVTDAENVG
     LYPDVQGMAT NLFFWSHTSM EESPDEVSWL NKHEISMTVA LVKHLLKQNY TTNDIVVLAT
     YSAQKNLMYR EYANVFGSTP DSNVIPVETV DSFQGKERKI VIVSLVRSHR GGRENTGIGF
     LAVANRICVA LTRAQHGMYI IGNGAYIMNN SELWNKIVNN LRRSNLIEYN LPLKCVAHGN
     IVTVKDPQDF ATKSPEGGCM QKCDTKKFCG HVCERLCHPN MEEEHLQRCL YNCDKKCSNP
     QFQHRCKKAC YEECGSCLYL VEVTLDCGHR ITTPCSRINS SKCDQSCTKK LLCGHACAAK
     CGEECTLVSE CSQLVGMPLS CGHIKQLTCS KISANEIDLT CDQRCEKTML ACPHKCAEIC
     GQPCTVECME VVNVTLGCSH SQDVVCSSFM PGMTDHIECL TKVPKTLSPC KHTELVLCKQ
     APSTKLCTRR CTSYLEKCGH TCENDCGICF TTKTHICQNM CQKVLNCGHT CSAKCGESCP
     PCKAFCTNKC EHQSCGAGER GFGRDCSKLC ALCVNNCSNK CAHRSCTLKC FEECNVKPCT
     EPCTDKLKCG HACLGICGEQ CPKICGTCER NKYIECVSGT SSTSRVHRLI MIPKCYHVFP
     VEVLDDHVKK QKEANEKLKC PKCSAFIVGV LRYARYTKKY YLNENMRKLE SNIRNIHQST
     LEGRVFQAVQ DSIGEIRNVT TNLTNASEDI LRNFHQKILD IRTSAETFKG KPEHKFKFAS
     LLQVANCCLA ITRLLSVSSK FRVSRRKDIP PTFDLMSVRV LGDMPFPKLI DELNRVNIHL
     SNTYETFMPG AIIPKLKWLI SRMTVLQQLT SMCHQLVLEK KDIADSDAHA INDACLNMFR
     YNEQHNYALN IENFEAIVVK VAPKLLEPTP KFWSWRRLQV PEL
 
 
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